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    OlsG (Sinac-1600) Is an ornithine lipid N-Methyltransferase from the planctomycete Singulisphaera acidiphila

    Access Status
    Open access via publisher
    Authors
    Escobedo-Hinojosa, W.
    Vences-Guzmán, M.
    Schubotz, F.
    Sandoval-Calderón, M.
    Summons, Roger
    López-Lara, I.
    Geiger, O.
    Sohlenkamp, C.
    Date
    2015
    Type
    Journal Article
    
    Metadata
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    Citation
    Escobedo-Hinojosa, W. and Vences-Guzmán, M. and Schubotz, F. and Sandoval-Calderón, M. and Summons, R. and López-Lara, I. and Geiger, O. et al. 2015. OlsG (Sinac-1600) Is an ornithine lipid N-Methyltransferase from the planctomycete Singulisphaera acidiphila. Journal of Biological Chemistry. 290 (24): pp. 15102-15111.
    Source Title
    Journal of Biological Chemistry
    DOI
    10.1074/jbc.M115.639575
    ISSN
    0021-9258
    URI
    http://hdl.handle.net/20.500.11937/33359
    Collection
    • Curtin Research Publications
    Abstract

    Ornithine lipids (OLs) are phosphorus-free membrane lipids widespread in bacteria but absent from archaea and eukaryotes. In addition to the unmodified OLs, a variety of OL derivatives hydroxylated in different structural positions has been reported. Recently, methylated derivatives of OLs were described in several planctomycetes isolated from a peat bog in Northern Russia, although the gene/enzyme responsible for the N-methylation of OL remained obscure. Here we identify and characterize the OL N-methyltransferase OlsG (Sinac-1600) from the planctomycete Singulisphaera acidiphila. When OlsG is co-expressed with the OL synthase OlsF in Escherichia coli, methylated OL derivatives are formed. An in vitro characterization shows that OlsG is responsible for the 3-fold methylation of the terminal d-nitrogen of OL. Methylation is dependent on the presence of the detergent Triton X-100 and the methyldonor S-adenosylmethionine.

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